Ovastacin, a cortical granule protease, cleaves ZP2 in the zona pellucida to prevent polyspermy

Burkart, Anna D.; Xiong, Bo; Baibakov, Boris; Jiménez-Movilla, María; Dean, Jurrien

doi:10.1083/jcb.201112094

Cited by 254 publications

(269 citation statements)

References 42 publications

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“…In fact, more recent work indicates that both purified mZP3 and mZP2 can bind to both AI and AR sperm (Kerr et al 2002). Furthermore, the supramolecular structure model of Dean et al argues that sperm would interact with both mZP3 and mZP2, provided that mZP2 is intact; only after a cleavage of mZP2 by a cortical granule protease to generate mZP2 f (Burkart et al 2012), sperm can no longer bind to the ZP (Gahlay et al 2010). Supporting the argument that the binding of mZP2 and mZP3 to sperm is a continuous event are the findings that a number of acrosomal proteins bind to the ZP (e.g.…”

Section: Discussionmentioning

confidence: 99%

“…More recently, Dean and colleagues present evidence that the supramolecular structure of the ZP, regulated by intactness of mZP2, is required for AI sperm binding (Rankin et al 2003, Gahlay et al 2010. Once mZP2 is cleaved at Ala166 to form mZP2 f , as occurring after fertilization (Burkart et al 2012), the ZP matrix becomes refractory to sperm binding (Florman & Ducibella 2006). Accumulated evidence also reveals the participation of acrosomal matrix proteins in ZP binding, a basis for how acrosome reacting sperm remain bound to the ZP (Kim & Gerton 2003, Buffone et al 2008a, 2008b.…”

Section: Introductionmentioning

confidence: 98%

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Sperm arylsulfatase A binds to mZP2 and mZP3 glycoproteins in a nonenzymatic manner

Xu¹,

Liu²,

Srakaew³

et al. 2012

Reproduction

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We have shown previously that sperm surface arylsulfatase A (ASA) of mouse, pig, and human is involved in sperm-egg zona pellucida (ZP) binding. By treating capacitated mouse sperm with A23187 to induce the acrosome reaction, we demonstrated by immunoblotting that ASA also existed in the acrosomal content and on the inner acrosomal membrane. Since mZP2 and mZP3 are known as sperm receptors, whereas mZP1 as a cross-linker of mZP2/mZP3, we determined whether purified ASA bound to mZP2 and mZP3 selectively. The three mZP glycoproteins were purified from solubilized ovarian ZP by size exclusion column chromatography. Immuno-dot blot analyses revealed that purified sperm ASA bound to mZP2 at the highest level followed by mZP3, whereas the binding of ASA to mZP1 was minimal. The results confirmed the physiological significance of sperm ASA in the ZP binding process. The binding of ASA to mZP2 and mZP3 was, however, not dependent on the active site pocket amino acids, Cys69, Lys123, and Lys302, which are pertinent to the capturing of an arylsulfate substrate, since ASA mutant with Ala substitution at these three residues still bound to mZP2 and mZP3. The availability of the active site pocket of ASA bound to the ZP suggested that ASA would still retain enzymatic activity, which might be important for subsequent sperm penetration through the ZP.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

Sperm arylsulfatase A binds to mZP2 and mZP3 glycoproteins in a nonenzymatic manner

Xu¹,

Liu²,

Srakaew³

et al. 2012

Reproduction

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“…With the penetration of the sperm into the egg, ovastacin is released from the egg's cortical granules and cleaves the zona pellucida 2 protein (ZP2) (Burkart et al 2012), leading to zona hardening and preventing polyspermy. In a recent study, ZP2 peptidetreated beads, deployed in the mouse female reproductive tract, act as a decoy to attract sperm and form binding, resulting in female infertility (Avella et al 2016).…”

Section: Fertilizationmentioning

confidence: 99%

Oviduct: roles in fertilization and early embryo development

Winuthayanon

2017

Journal of Endocrinology

208

191

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Animal oviducts and human Fallopian tubes are a part of the female reproductive tract that hosts fertilization and pre-implantation development of the embryo. With an increasing understanding of roles of the oviduct at the cellular and molecular levels, current research signifies the importance of the oviduct on naturally conceived fertilization and pre-implantation embryo development. This review highlights the physiological conditions within the oviduct during fertilization, environmental regulation, oviductal fluid composition and its role in protecting embryos and supplying nutrients. Finally, the review compares different aspects of naturally occurring fertilization and assisted reproductive technology (ART)-achieved fertilization and embryo development, giving insight into potential areas for improvement in this technology.

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“…These results indicated that ZP3 is the sperm binding protein in the pvm of both chicken and quail, though the detailed mechanism was not known. In mice, it was reported that ZP2 also supports the sperm binding (Bleil et al, 1988), and the structural change of the ZP2 as a result of limited digestion by the cortical granule protease protects the polyspermic fertilization (Burkart et al, 2012). In birds, ZP2 is expressed in the oocyte of immature follicles and exists in the pvm as a minor component (Kinoshita et al, 2010).…”

Section: Sperm-egg Bindingmentioning

confidence: 99%

“…protein so sperm no longer interacted with such ovastatinmodified zona pellucida in mice (Burkart et al, 2012). In the case of Xenopus laevis fertilization, soon after the entry of the first sperm into the egg, the egg's plasma membrane quickly changes to initiate a fast block to polyspermy by eliciting a positive-going fertilization potential to prevent the fusion of a second sperm (Elinson, 1986;Iwao, 2000;Wong and Wessel, 2006).…”

Section: Protease Responsible For Pvm Digestionmentioning

confidence: 99%

Sperm-Egg Interaction during Fertilization in Birds

et al. 2016

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Fertilization in animals that employ sexual reproduction is an indispensable event for the production of the next generation. A significant advancement in our understanding of the molecular mechanisms of sperm-egg interaction in mammalian species was achieved in the last few decades. However, the same level of knowledge has not been accumulated for birds because of egg size and the difficulty in mimicking the physiological polyspermy that takes place during normal fertilization. In this review, we summarize the current understanding of sperm-egg interaction mechanism during fertilization in birds, especially focusing on sperm-egg binding, sperm acrosome reaction and the authentic sperm protease required for the hole formation on the perivitelline membrane. We explain that the zona pellucida proteins (ZP1 and ZP3) in the perivitelline membrane play important roles in sperm-egg binding, induction of the acrosome reaction as well as sperm penetration by digestion of sperm protease. We anticipate that a deeper understanding of avian fertilization will open up new avenues to create powerful tools for a myriad of applications in the poultry industries including the production of transgenic and cloned birds.

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Ovastacin, a cortical granule protease, cleaves ZP2 in the zona pellucida to prevent polyspermy

Abstract: After fertilization, the metalloendoprotease ovastacin is released by cortical granule exocytosis and cleaves the zona pellucida glycoprotein ZP2, an essential step to block sperm binding to an already fertilized egg.

Cited by 254 publications

References 42 publications

Sperm arylsulfatase A binds to mZP2 and mZP3 glycoproteins in a nonenzymatic manner

Sperm arylsulfatase A binds to mZP2 and mZP3 glycoproteins in a nonenzymatic manner

Oviduct: roles in fertilization and early embryo development

Sperm-Egg Interaction during Fertilization in Birds

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